ID W0F0I9_9BACT Unreviewed; 795 AA.
AC W0F0I9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:AHF15338.1};
GN ORFNames=NIASO_09590 {ECO:0000313|EMBL:AHF15338.1};
OS Niabella soli DSM 19437.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niabella.
OX NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF15338.1, ECO:0000313|Proteomes:UP000003586};
RN [1] {ECO:0000313|EMBL:AHF15338.1, ECO:0000313|Proteomes:UP000003586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP007035; AHF15338.1; -; Genomic_DNA.
DR RefSeq; WP_008584265.1; NZ_CP007035.1.
DR AlphaFoldDB; W0F0I9; -.
DR STRING; 929713.NIASO_09590; -.
DR KEGG; nso:NIASO_09590; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_350462_0_0_10; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000003586; Chromosome.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003586}.
FT DOMAIN 471..645
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 795 AA; 88685 MW; 60B00DDB21D9BFD7 CRC64;
MEHNTSDLIT STNMLSFDKF KDGVLHDYYV ASLSRETSLL GRREVLTGKA KFGIFGDGKE
VAQVAMSKFF QPGDWRSGYY RDQTLMFAIG VGTPQQYFAQ LYADPDPQNE PFSVGRQMNS
HYTSRNADAE GNWLDLVHIK NTATDMAPTA AQMPRSYGLA YASKCFREIP ELQQFTNLSN
NGNEVCFCTI GDASTSEGHF WEIVNAAGVA QIPLVIFVWD DGYGISVPRE LQTTKGSISE
ALKGFEKEEG TNGFYIQKVK GWDYMGMIEA FEEGISLARE THTPVIFHVD ELTQPQGHST
SGSHERYKSP ERLEWERERD CLKKLKEWIL KNGLSDEATL EKIEQDARAN VKDARDKAWK
DYIKPIKAQV ETTRNILNEL AEQLPEKAGD IKKLLPDLVT NREPLRKNVL QTLYKAILIG
GNQAVTAQQY YDTLCAENAV IYNSNLYDEG PKSALKVKPV APVVTADSPV LNGYEILNHY
FDQLFSNNPK VIAFGEDLGK IGDVNQGFAG LQKKHGPERI ADTGIRELSI MGRGIGLALR
GLRPIAEIQY LDYLVYGLQP LTDDVASLQY RTGGQQFCPL IVRSRGHRLE GIWHSGSPMG
MIINSLRGIH ICVPRNMVQA AAMYNTLLQS NDPGLVIESL NGYRLKEKLP ENLDTMTLAF
GVPEILHPGT DITIVSYGST LRVIQEAIKI VEPLGVSCEL IDVQTLLPFD IHHSILHSLK
KTNRIVFIDE DVPGGATAFM LTKVIEEQGG YRHLDVAPRT ITAKEHRPGY GSDGDYFSKP
NAEEVAATLL DMMKE
//
